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Conserved domains on  [gi|1833567697|emb|CAB3447288|]
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unnamed protein product [Digitaria exilis]

Protein Classification

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List of domain hits

 Name Accession Description Interval E-value
Ubl_UBL5 cd01791
ubiquitin-like (Ubl) domain found in ubiquitin-like protein 5 (UBL5) and similar proteins; ...
 1252-1322 1.74e-49

ubiquitin-like (Ubl) domain found in ubiquitin-like protein 5 (UBL5) and similar proteins; UBL5, known as Hub1 in yeast, is an atypical ubiquitin-like (Ubl) post-translational modifier that contains a conserved Ubl domain with a beta-grasp Ubl fold. At the C-terminal end of its Ubl fold is a di-tyrosine motif followed by a single variable residue instead of the characteristic di-glycine found in all other Ubl modifiers, and thus UBL5 does not form covalent conjugates with cellular proteins. The yeast Hub1p binds non-covalently to the HIND element of spliceosomal protein Snu66p (Snu66p is termed SART1 in mammals) and modifies the spliceosome by this unconventional Ubl modifier. In higher eukaryotes, UBL5/Hub1 plays a role in modulating pre-mRNA splicing. It also is required for signaling in the mitochondrial unfolded protein response, through interaction with the transcription factor DVE-1 and upregulation of chaperone genes in response to mitochondrial stress. Moreover, UBL5 functions as a factor that directly binds to and stabilizes FANCI, and promotes the functionality of the Fanconi anemia (FA) DNA repair pathway.


:

Pssm-ID: 340489  Cd Length: 71  Bit Score: 169.42  E-value: 1.74e-49
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1833567697 1252 MIEVVLNDRLGKKVRVKCNEDDTIGDLKRLVAAQTGTRAEKIRIQKWYTIYKDHITLADYEIHDGMGLELY 1322
Cdd:cd01791      1 MIEVICNDRLGKKVRVKCNPDDTIGDLKKLIAAQTGTRPEKIVLKKWYTIFKDHITLEDYEIHDGMNLELY 71
Senescence_reg pfam04520
Senescence regulator; This protein regulates the expression of proteins associated with leaf ...
 869-1006 3.93e-23

Senescence regulator; This protein regulates the expression of proteins associated with leaf senescence in plants.


:

Pssm-ID: 461341  Cd Length: 171  Bit Score: 97.54  E-value: 3.93e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833567697  869 EEFDESEIWGAFAAPSAFPAD-------------------------------PPPSRALPLPLGAWKGAAATKPPVRGGG 917
Cdd:pfam04520    1 EELDEEDVWWSAAGDEDPDSQddppasqssdgewdgglsaalpedestssssSSSSAARAIPAAPPRPRPASPSGKRPSG 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833567697  918 RAAAHGSLPVNIPDWSKILGDEYRAHHGSagdwevDDGDDEDGGVADAVVVPPHELAWRRR-RAASLSVHEGagvVGRTL 996
Cdd:pfam04520   81 GPRDAQSAPVNVPDWSKILGASSSRRSRH------DDDDGDDDEDDGAEMVPPHEYVARRRaQMASFSVLEG---AGRTL 151

                          170
                   ....*....|....*.
gi 1833567697  997 K------VRDAVWKRT 1006
Cdd:pfam04520  152 KgrdlrrVRNAVLRQT 167
PHA03247 super family cl33720
large tegument protein UL36; Provisional
 463-696 1.27e-03

large tegument protein UL36; Provisional


The actual alignment was detected with superfamily member PHA03247:

Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 43.39  E-value: 1.27e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833567697  463 THALHHPRPAPCQAATCAPvhvgahnhfdayGASATATVRTKHSLTSPGPGWPSRPRsrhpiRREALHRLSSRAAALSRR 542
Cdd:PHA03247  2621 THAPDPPPPSPSPAANEPD------------PHPPPTVPPPERPRDDPAPGRVSRPR-----RARRLGRAAQASSPPQRP 2683

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833567697  543 TPRVAPERVGILRALSRGDANPsdsamsRTTKPWTRPTRTWARVLHGRIHSRFATYAAADGPVfrRRGLPLRPKRPATQR 622
Cdd:PHA03247  2684 RRRAARPTVGSLTSLADPPPPP------PTPEPAPHALVSATPLPPGPAAARQASPALPAAPA--PPAVPAGPATPGGPA 2755

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1833567697  623 SSPPPPLHQTGPicRHAADNDPAGARTGRTT--CVPDLARYTSDMGPHWSISQPKGESKVRRLTPTTHKSQSGRLP 696
Cdd:PHA03247  2756 RPARPPTTAGPP--APAPPAAPAAGPPRRLTrpAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLP 2829
 
Name Accession Description Interval E-value
Ubl_UBL5 cd01791
ubiquitin-like (Ubl) domain found in ubiquitin-like protein 5 (UBL5) and similar proteins; ...
 1252-1322 1.74e-49

ubiquitin-like (Ubl) domain found in ubiquitin-like protein 5 (UBL5) and similar proteins; UBL5, known as Hub1 in yeast, is an atypical ubiquitin-like (Ubl) post-translational modifier that contains a conserved Ubl domain with a beta-grasp Ubl fold. At the C-terminal end of its Ubl fold is a di-tyrosine motif followed by a single variable residue instead of the characteristic di-glycine found in all other Ubl modifiers, and thus UBL5 does not form covalent conjugates with cellular proteins. The yeast Hub1p binds non-covalently to the HIND element of spliceosomal protein Snu66p (Snu66p is termed SART1 in mammals) and modifies the spliceosome by this unconventional Ubl modifier. In higher eukaryotes, UBL5/Hub1 plays a role in modulating pre-mRNA splicing. It also is required for signaling in the mitochondrial unfolded protein response, through interaction with the transcription factor DVE-1 and upregulation of chaperone genes in response to mitochondrial stress. Moreover, UBL5 functions as a factor that directly binds to and stabilizes FANCI, and promotes the functionality of the Fanconi anemia (FA) DNA repair pathway.


Pssm-ID: 340489  Cd Length: 71  Bit Score: 169.42  E-value: 1.74e-49
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1833567697 1252 MIEVVLNDRLGKKVRVKCNEDDTIGDLKRLVAAQTGTRAEKIRIQKWYTIYKDHITLADYEIHDGMGLELY 1322
Cdd:cd01791      1 MIEVICNDRLGKKVRVKCNPDDTIGDLKKLIAAQTGTRPEKIVLKKWYTIFKDHITLEDYEIHDGMNLELY 71
Senescence_reg pfam04520
Senescence regulator; This protein regulates the expression of proteins associated with leaf ...
 869-1006 3.93e-23

Senescence regulator; This protein regulates the expression of proteins associated with leaf senescence in plants.


Pssm-ID: 461341  Cd Length: 171  Bit Score: 97.54  E-value: 3.93e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833567697  869 EEFDESEIWGAFAAPSAFPAD-------------------------------PPPSRALPLPLGAWKGAAATKPPVRGGG 917
Cdd:pfam04520    1 EELDEEDVWWSAAGDEDPDSQddppasqssdgewdgglsaalpedestssssSSSSAARAIPAAPPRPRPASPSGKRPSG 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833567697  918 RAAAHGSLPVNIPDWSKILGDEYRAHHGSagdwevDDGDDEDGGVADAVVVPPHELAWRRR-RAASLSVHEGagvVGRTL 996
Cdd:pfam04520   81 GPRDAQSAPVNVPDWSKILGASSSRRSRH------DDDDGDDDEDDGAEMVPPHEYVARRRaQMASFSVLEG---AGRTL 151

                          170
                   ....*....|....*.
gi 1833567697  997 K------VRDAVWKRT 1006
Cdd:pfam04520  152 KgrdlrrVRNAVLRQT 167
ubiquitin pfam00240
Ubiquitin family; This family contains a number of ubiquitin-like proteins: SUMO (smt3 homolog) ...
 1262-1322 2.68e-06

Ubiquitin family; This family contains a number of ubiquitin-like proteins: SUMO (smt3 homolog), Nedd8, Elongin B, Rub1, and Parkin. A number of them are thought to carry a distinctive five-residue motif termed the proteasome-interacting motif (PIM), which may have a biologically significant role in protein delivery to proteasomes and recruitment of proteasomes to transcription sites.


Pssm-ID: 459726 [Multi-domain]  Cd Length: 72  Bit Score: 46.40  E-value: 2.68e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1833567697 1262 GKKVRVKCNEDDTIGDLKRLVAAQTGTRAEKIRIqkwytIYK-----DHITLADYEIHDGMGLELY 1322
Cdd:pfam00240    8 GKKITLEVDPTDTVLELKEKIAEKEGVPPEQQRL-----IYSgkvleDDQTLGEYGIEDGSTIHLV 68
UBQ smart00213
Ubiquitin homologues; Ubiquitin-mediated proteolysis is involved in the regulated turnover of ...
 1262-1322 4.47e-04

Ubiquitin homologues; Ubiquitin-mediated proteolysis is involved in the regulated turnover of proteins required for controlling cell cycle progression


Pssm-ID: 214563 [Multi-domain]  Cd Length: 72  Bit Score: 39.93  E-value: 4.47e-04
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1833567697  1262 GKKVRVKCNEDDTIGDLKRLVAAQTGTRAEKIRIqkwytIY-----KDHITLADYEIHDGMGLELY 1322
Cdd:smart00213   10 GKTITLEVKPSDTVSELKEKIAELTGIPPEQQRL-----IYkgkvlEDDRTLADYGIQDGSTIHLV 70
PHA03247 PHA03247
large tegument protein UL36; Provisional
 463-696 1.27e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 43.39  E-value: 1.27e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833567697  463 THALHHPRPAPCQAATCAPvhvgahnhfdayGASATATVRTKHSLTSPGPGWPSRPRsrhpiRREALHRLSSRAAALSRR 542
Cdd:PHA03247  2621 THAPDPPPPSPSPAANEPD------------PHPPPTVPPPERPRDDPAPGRVSRPR-----RARRLGRAAQASSPPQRP 2683

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833567697  543 TPRVAPERVGILRALSRGDANPsdsamsRTTKPWTRPTRTWARVLHGRIHSRFATYAAADGPVfrRRGLPLRPKRPATQR 622
Cdd:PHA03247  2684 RRRAARPTVGSLTSLADPPPPP------PTPEPAPHALVSATPLPPGPAAARQASPALPAAPA--PPAVPAGPATPGGPA 2755

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1833567697  623 SSPPPPLHQTGPicRHAADNDPAGARTGRTT--CVPDLARYTSDMGPHWSISQPKGESKVRRLTPTTHKSQSGRLP 696
Cdd:PHA03247  2756 RPARPPTTAGPP--APAPPAAPAAGPPRRLTrpAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLP 2829
 
Name Accession Description Interval E-value
Ubl_UBL5 cd01791
ubiquitin-like (Ubl) domain found in ubiquitin-like protein 5 (UBL5) and similar proteins; ...
 1252-1322 1.74e-49

ubiquitin-like (Ubl) domain found in ubiquitin-like protein 5 (UBL5) and similar proteins; UBL5, known as Hub1 in yeast, is an atypical ubiquitin-like (Ubl) post-translational modifier that contains a conserved Ubl domain with a beta-grasp Ubl fold. At the C-terminal end of its Ubl fold is a di-tyrosine motif followed by a single variable residue instead of the characteristic di-glycine found in all other Ubl modifiers, and thus UBL5 does not form covalent conjugates with cellular proteins. The yeast Hub1p binds non-covalently to the HIND element of spliceosomal protein Snu66p (Snu66p is termed SART1 in mammals) and modifies the spliceosome by this unconventional Ubl modifier. In higher eukaryotes, UBL5/Hub1 plays a role in modulating pre-mRNA splicing. It also is required for signaling in the mitochondrial unfolded protein response, through interaction with the transcription factor DVE-1 and upregulation of chaperone genes in response to mitochondrial stress. Moreover, UBL5 functions as a factor that directly binds to and stabilizes FANCI, and promotes the functionality of the Fanconi anemia (FA) DNA repair pathway.


Pssm-ID: 340489  Cd Length: 71  Bit Score: 169.42  E-value: 1.74e-49
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1833567697 1252 MIEVVLNDRLGKKVRVKCNEDDTIGDLKRLVAAQTGTRAEKIRIQKWYTIYKDHITLADYEIHDGMGLELY 1322
Cdd:cd01791      1 MIEVICNDRLGKKVRVKCNPDDTIGDLKKLIAAQTGTRPEKIVLKKWYTIFKDHITLEDYEIHDGMNLELY 71
Senescence_reg pfam04520
Senescence regulator; This protein regulates the expression of proteins associated with leaf ...
 869-1006 3.93e-23

Senescence regulator; This protein regulates the expression of proteins associated with leaf senescence in plants.


Pssm-ID: 461341  Cd Length: 171  Bit Score: 97.54  E-value: 3.93e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833567697  869 EEFDESEIWGAFAAPSAFPAD-------------------------------PPPSRALPLPLGAWKGAAATKPPVRGGG 917
Cdd:pfam04520    1 EELDEEDVWWSAAGDEDPDSQddppasqssdgewdgglsaalpedestssssSSSSAARAIPAAPPRPRPASPSGKRPSG 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833567697  918 RAAAHGSLPVNIPDWSKILGDEYRAHHGSagdwevDDGDDEDGGVADAVVVPPHELAWRRR-RAASLSVHEGagvVGRTL 996
Cdd:pfam04520   81 GPRDAQSAPVNVPDWSKILGASSSRRSRH------DDDDGDDDEDDGAEMVPPHEYVARRRaQMASFSVLEG---AGRTL 151

                          170
                   ....*....|....*.
gi 1833567697  997 K------VRDAVWKRT 1006
Cdd:pfam04520  152 KgrdlrrVRNAVLRQT 167
Ubl_ubiquitin_like cd17039
ubiquitin-like (Ubl) domain found in ubiquitin and ubiquitin-like Ubl proteins; Ubiquitin-like ...
 1255-1316 5.08e-08

ubiquitin-like (Ubl) domain found in ubiquitin and ubiquitin-like Ubl proteins; Ubiquitin-like (Ubl) proteins have a similar ubiquitin (Ub) beta-grasp fold and attach to other proteins in a Ubl manner but with biochemically distinct roles. Ub and Ubl proteins conjugate and deconjugate via ligases and peptidases to covalently modify target polypeptides. Some Ubl domains have adaptor roles in Ub-signaling by mediating protein-protein interaction. Prokaryotic sulfur carrier proteins are Ub-related proteins that can be activated in an ATP-dependent manner. Polyubiquitination signals for a diverse set of cellular events via different isopeptide linkages formed between the C terminus of one ubiquitin (Ub) and the epsilon-amine of K6, K11, K27, K29, K33, K48, or K63 of a second Ub. One of these seven lysine residues (K27, Ub numbering) is conserved in this Ubl_ubiquitin_like family. K27-linked Ub chains are versatile and can be recognized by several downstream receptor proteins. K27 has roles beyond chain linkage, such as in Ubl NEDD8 (which contains many of the same lysines (K6, K11, K27, K33, K48) as Ub) where K27 has a role (other than conjugation) in the mechanism of protein neddylation.


Pssm-ID: 340559 [Multi-domain]  Cd Length: 68  Bit Score: 51.06  E-value: 5.08e-08
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1833567697 1255 VVLNDRLGKKVRVKCNEDDTIGDLKRLVAAQTGTRAEKIRIQKWYTIYKDHITLADYEIHDG 1316
Cdd:cd17039      1 ITVKTLDGKTYTVEVDPDDTVADLKEKIEEKTGIPVEQQRLIYNGKELKDDKTLSDYGIKDG 62
ubiquitin pfam00240
Ubiquitin family; This family contains a number of ubiquitin-like proteins: SUMO (smt3 homolog) ...
 1262-1322 2.68e-06

Ubiquitin family; This family contains a number of ubiquitin-like proteins: SUMO (smt3 homolog), Nedd8, Elongin B, Rub1, and Parkin. A number of them are thought to carry a distinctive five-residue motif termed the proteasome-interacting motif (PIM), which may have a biologically significant role in protein delivery to proteasomes and recruitment of proteasomes to transcription sites.


Pssm-ID: 459726 [Multi-domain]  Cd Length: 72  Bit Score: 46.40  E-value: 2.68e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1833567697 1262 GKKVRVKCNEDDTIGDLKRLVAAQTGTRAEKIRIqkwytIYK-----DHITLADYEIHDGMGLELY 1322
Cdd:pfam00240    8 GKKITLEVDPTDTVLELKEKIAEKEGVPPEQQRL-----IYSgkvleDDQTLGEYGIEDGSTIHLV 68
Ubl_Dsk2p_like cd16106
ubiquitin-like (Ubl) domain found in Saccharomyces cerevisiae proteasome interacting protein ...
 1262-1316 8.02e-05

ubiquitin-like (Ubl) domain found in Saccharomyces cerevisiae proteasome interacting protein Dsk2p and similar proteins; The family contains several fungal multiubiquitin receptors, including Saccharomyces cerevisiae Dsk2p and Schizosaccharomyces pombe Dph1p, both of which have been characterized as shuttle proteins transporting ubiquitinated substrates destined for degradation from the E3 ligase to the 26S proteasome. They interact with the proteasome through their N-terminal ubiquitin-like domain (Ubl) and with ubiquitin (Ub) through their C-terminal Ub-associated domain (UBA). S. cerevisiae Dsk2p is a nuclear-enriched protein that may involve in the ubiquitin-proteasome proteolytic pathway through interacting with K48-linked polyubiquitin and the proteasome. Moreover, it has been implicated in spindle pole duplication through assisting in Cdc31 assembly into the new spindle pole body (SPB). S. pombe Dph1p is an ubiquitin (Ub0 receptor working in concert with the class V myosin, Myo52, to target the degradation of the S. pombe CLIP-170 homolog, Tip1. It also can protect Ub chains against disassembly by deubiquitinating enzymes.


Pssm-ID: 340523 [Multi-domain]  Cd Length: 73  Bit Score: 42.24  E-value: 8.02e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833567697 1262 GKKVRVKCNEDDTIGDLKRLVAAQTGTRAEKIRIqkwytIYKDHI-----TLADYEIHDG 1316
Cdd:cd16106     10 GKKFTVEVEPDATVLELKELIAEKSDIPAEQQRL-----IYKGKIlkdeeTLSSYKIQDG 64
UBQ smart00213
Ubiquitin homologues; Ubiquitin-mediated proteolysis is involved in the regulated turnover of ...
 1262-1322 4.47e-04

Ubiquitin homologues; Ubiquitin-mediated proteolysis is involved in the regulated turnover of proteins required for controlling cell cycle progression


Pssm-ID: 214563 [Multi-domain]  Cd Length: 72  Bit Score: 39.93  E-value: 4.47e-04
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1833567697  1262 GKKVRVKCNEDDTIGDLKRLVAAQTGTRAEKIRIqkwytIY-----KDHITLADYEIHDGMGLELY 1322
Cdd:smart00213   10 GKTITLEVKPSDTVSELKEKIAELTGIPPEQQRL-----IYkgkvlEDDRTLADYGIQDGSTIHLV 70
PHA03247 PHA03247
large tegument protein UL36; Provisional
 463-696 1.27e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 43.39  E-value: 1.27e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833567697  463 THALHHPRPAPCQAATCAPvhvgahnhfdayGASATATVRTKHSLTSPGPGWPSRPRsrhpiRREALHRLSSRAAALSRR 542
Cdd:PHA03247  2621 THAPDPPPPSPSPAANEPD------------PHPPPTVPPPERPRDDPAPGRVSRPR-----RARRLGRAAQASSPPQRP 2683

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833567697  543 TPRVAPERVGILRALSRGDANPsdsamsRTTKPWTRPTRTWARVLHGRIHSRFATYAAADGPVfrRRGLPLRPKRPATQR 622
Cdd:PHA03247  2684 RRRAARPTVGSLTSLADPPPPP------PTPEPAPHALVSATPLPPGPAAARQASPALPAAPA--PPAVPAGPATPGGPA 2755

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1833567697  623 SSPPPPLHQTGPicRHAADNDPAGARTGRTT--CVPDLARYTSDMGPHWSISQPKGESKVRRLTPTTHKSQSGRLP 696
Cdd:PHA03247  2756 RPARPPTTAGPP--APAPPAAPAAGPPRRLTrpAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLP 2829
Ubl_SF3a120 cd01800
ubiquitin-like (Ubl) domain found in splicing factor 3A 120kDa subunit (SF3a120) and similar ...
 1273-1321 1.88e-03

ubiquitin-like (Ubl) domain found in splicing factor 3A 120kDa subunit (SF3a120) and similar proteins; Mammalian splicing factor SF3a consists of three subunits of 60, 66, and 120 kDa and functions early during pre-mRNA splicing by converting the U2 snRNP to its active form. The 120kDa subunit SF3a120, also termed splicing factor 3A subunit 1 (SF3A1), or spliceosome-associated protein 114 (SAP114), is the U2 snRNP-specific protein that is critical for spliceosome assembly and normal splicing events. During splicing, SF3a120, together with the U2 snRNP and other proteins, are recruited to the 3' splicing site to generate the splicing complex A after the recognition of the 3' splicing site. SF3a120 contains two N-terminal SWAP (suppressor-of-white-apricot) domains, referred to collectively as the SURP module, as well as a C-terminal ubiquitin-like (Ubl) domain with a beta-grasp Ubl fold, a common structure involved in protein-protein interactions.


Pssm-ID: 340498  Cd Length: 84  Bit Score: 38.71  E-value: 1.88e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 1833567697 1273 DTIGDLKRLVAAQTGTRAEKIRIQ-KWYTIYKDHITLADYEIHDGMGLEL 1321
Cdd:cd01800     32 DTISVLKEKIHEELGMPANKQKLQvEGGGFLKDSNSLAFYNLGSGTVLTL 81
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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